A point mutation in the neu oncogene mimics ligand induction of receptor aggregation.
about
Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent associationA hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factorErbB receptors: from oncogenes to targeted cancer therapiesHER-2 overexpression differentially alters transforming growth factor-beta responses in luminal versus mesenchymal human breast cancer cellsTransmembrane helix dimerization: beyond the search for sequence motifsStructural Evidence for Loose Linkage between Ligand Binding and Kinase Activation in the Epidermal Growth Factor ReceptorActivating point mutations in the common beta subunit of the human GM-CSF, IL-3 and IL-5 receptors suggest the involvement of beta subunit dimerization and cell type-specific molecules in signallingCorrelation of the structure of the transmembrane domain of the neu oncogene-encoded p185 protein with its functionThe glucocorticoid receptor type II complex is a target of the HIV-1 vpr gene productMultiple consequences of a single amino acid pathogenic RTK mutation: the A391E mutation in FGFR3Distinct tyrosine autophosphorylation sites negatively and positively modulate neu-mediated transformationConstitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasiaDominant-negative mutants of Grb2 induced reversal of the transformed phenotypes caused by the point mutation-activated rat HER-2/NeuControlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimersCharacterization of membrane protein interactions in plasma membrane derived vesicles with quantitative imaging Förster resonance energy transferThe ErbB signaling network: receptor heterodimerization in development and cancerA putative molecular-activation switch in the transmembrane domain of erbB2.Three dimensional structure of the transmembrane region of the proto-oncogenic and oncogenic forms of the neu protein.Effect of the G375C and G346E achondroplasia mutations on FGFR3 activation.In vivo selection for metastasis promoting genes in the mouseInhibition of eIF2alpha dephosphorylation inhibits ErbB2-induced deregulation of mammary acinar morphogenesisDifferential binding patterns of monoclonal antibody 2C4 to the ErbB3-p185her2/neu and the EGFR-p185her2/neu complexes.Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.Molecular mechanisms of acquired resistance to tyrosine kinase targeted therapyOncogenic activating mutations in the neu/erbB-2 oncogene are involved in the induction of mammary tumors.A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFR beta oncoprotein.Bivalence of EGF-like ligands drives the ErbB signaling networkInsulin receptor activation with transmembrane domain ligands.Differential endocytic routing of homo- and hetero-dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers.A single amino acid substitution in a WW-like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation.Elevated expression of activated forms of Neu/ErbB-2 and ErbB-3 are involved in the induction of mammary tumors in transgenic mice: implications for human breast cancerc-erbB2-induced disruption of matrix adhesion and morphogenesis reveals a novel role for protein kinase B as a negative regulator of alpha(2)beta(1) integrin function.A subdomain in the transmembrane domain is necessary for p185neu* activation.Driving forces for transmembrane alpha-helix oligomerization.High-throughput selection of transmembrane sequences that enhance receptor tyrosine kinase activationReceptor-like protein tyrosine phosphatase alpha homodimerizes on the cell surface.gammadeltaTCR ligands and lineage commitment.HER2/neu: mechanisms of dimerization/oligomerization.A kinase associated with chromatin that can be activated by ligand-p185c-Neu or epidermal growth factor-receptor interactions.Molecular Dynamics Simulations of Micelle Formation around Dimeric Glycophorin A Transmembrane Helices.
P2860
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P2860
A point mutation in the neu oncogene mimics ligand induction of receptor aggregation.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh-hant
name
A point mutation in the neu oncogene mimics ligand induction of receptor aggregation.
@en
A point mutation in the neu oncogene mimics ligand induction of receptor aggregation.
@nl
type
label
A point mutation in the neu oncogene mimics ligand induction of receptor aggregation.
@en
A point mutation in the neu oncogene mimics ligand induction of receptor aggregation.
@nl
prefLabel
A point mutation in the neu oncogene mimics ligand induction of receptor aggregation.
@en
A point mutation in the neu oncogene mimics ligand induction of receptor aggregation.
@nl
P2093
P356
P1433
P1476
A point mutation in the neu oncogene mimics ligand induction of receptor aggregation.
@en
P2093
P2888
P304
P356
10.1038/339230A0
P407
P577
1989-05-01T00:00:00Z
P6179
1049500705